Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis [PDF]
Frontiers in Molecular Biosciences, 2017 Here, we review the diverse roles and functions of AAA+ protease complexes in protein homeostasis, control of stress response and cellular development pathways by regulatory and general proteolysis in the Gram-positive model organism Bacillus subtilis ...
Alexander K. W. Elsholz +5 more
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The Mitochondrial m-AAA Protease Prevents Demyelination and Hair Greying. [PDF]
PLoS Genetics, 2016 The m-AAA protease preserves proteostasis of the inner mitochondrial membrane. It ensures a functional respiratory chain, by controlling the turnover of respiratory complex subunits and allowing mitochondrial translation, but other functions in ...
Shuaiyu Wang +7 more
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Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state [PDF]
Communications Biology, 2022 Liu et. al determine the cryo-EM structure of ADP-bound transmembrane AAA+ protease FtsH and provide insights into conformational switches between different nucleotide states important for ATP hydrolysis by FtsH.
Wu Liu +4 more
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AAA+ protease-adaptor structures reveal altered conformations and ring specialization. [PDF]
Nat Struct Mol Biol, 2022 ClpAP, a two-ring AAA+ protease, degrades N-end-rule proteins bound by the ClpS adaptor. Here, we present high-resolution cryo-EM structures of ClpAPS complexes showing how ClpA pore loops interact with the ClpS N-terminal extension (NTE), which is ...
Kim S, Fei X, Sauer RT, Baker TA.
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Structural basis for distinct operational modes and protease activation in AAA+ protease Lon. [PDF]
Sci Adv, 2020 Substrate-free and -bound states of Lon reveal distinct operational modes used by the enzyme to process protein substrates. Substrate-bound structures of AAA+ protein translocases reveal a conserved asymmetric spiral staircase architecture wherein a ...
Shin M +7 more
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Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease [PDF]
Cell Reports, 2023 Summary: Lon is a widely distributed AAA+ (ATPases associated with diverse cellular activities) protease known for degrading poorly folded and damaged proteins and is often classified as a weak protein unfoldase.
Meghann R. Kasal +6 more
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Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP [PDF]
Communications BiologyBacterial AAA+ proteases are composed of a AAA+ partner (e.g., ClpC) and an associated peptidase (e.g., ClpP). They represent ATP-fuelled and self-compartmentalized proteolytic machines that are crucial for stress resistance and virulence.
Stavros Azinas +6 more
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Structure, function, and substrates of Clp AAA+ protease systems in cyanobacteria, plastids, and apicoplasts: A comparative analysis. [PDF]
J Biol Chem, 2021 ATPases Associated with diverse cellular Activities (AAA+) are a superfamily of proteins that typically assemble into hexameric rings. These proteins contain AAA+ domains with two canonical motifs (Walker A and B) that bind and hydrolyze ATP, allowing ...
Bouchnak I, van Wijk KJ.
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The cytoplasmic domain of the AAA+ protease FtsH is tilted with respect to the membrane to facilitate substrate entry. [PDF]
J Biol Chem, 2021 AAA+ proteases are degradation machines that use ATP hydrolysis to unfold protein substrates and translocate them through a central pore toward a degradation chamber.
Carvalho V +8 more
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Mitochondrial Phospholipid Homeostasis Is Regulated by the i-AAA Protease PaIAP and Affects Organismic Aging. [PDF]
Cells, 2021 Mitochondria are ubiquitous organelles of eukaryotic organisms with a number of essential functions, including synthesis of iron-sulfur clusters, amino acids, lipids, and adenosine triphosphate (ATP).
Löser T +3 more
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